Attachment of Lipase on Amino Functionalized Titania Submicrospheres via Covalent Binding

• 作 者: WU Hong LIANG Yan-peng SHI Jia-fu WANG Xiao-li
• 机 构: School of Chemical Engineering and Technology,Tianjin University,
• 出 处: 化学工业与工程
• 发表日期: 2013年02期
• 关键词: lipase titania covalently immobilization linking recycling dopamine incubation M

A facile and effective method for immobilized lipase was presented.The titania submicrospheres were synthesized via a modified sol-gel method followed by amino functionalization through the chelation between dopamine and titania.Lipase was covalently attached on the functionalized titania surface using glutaraldehyde as the cross linking agent.The loading ratio and relative activity of the immobilized lipase were 230 mg/g titania submicrospheres and 65%,respectively.The kinetic parameters including the Michaelis constant(Km) and the maximum reaction rate(Vmax) changed slightly after immobilization.Compared to free lipase,the immobilized lipase showed favorable pH stability,thermostability,recycling stability and storage stability.The immobilized lipase retained 90% activity after incubation at 50 ℃ for 2 h,while the free lipase retained only 60% activity.The immobilized lipase retained more than 80% activity after 8 batches.

A facile and effective method for immobilized lipase was presented. The titania submicrospheres were synthesized via a modified sol-gel method followed by amino functionalization through the chelation between dopamine and titania. Lipase was covalently attached on the functionalized titania surface using glutaraldehyde as the cross linking agent. The loading ratio and relative activity of the immobilized lipase were 230 mg / g titania submicrospheres and 65%, respectively. kinetic parameters including the Michaelis constant (Km) and the maximum reaction rate (Vmax) changed slightly after immobilization. Compared to free lipase, the immobilized lipase showed favorable pH stability, thermostability, recycling stability and storage stability.The immobilized lipase retained 90% activity after incubation at 50 ℃ for 2 h, while the free lipase retained only 60% activity. than 80% activity after 8 batches.